Raman Spectroscopy of Proteins

The sections in this article are Introduction General Aspects of Ordinary Raman Spectra of Proteins Amides I and III Frequencies and Secondary Structures Trp Bands and Microenvironments of Trp Residues Tyr Bands and Hydrogen Bonding Histidine Band and Protonation SS Stretching Frequency and Conformation of Disulfide Bridge UV Resonance Raman Spectra of Proteins Amide Modes Tyrosine-Related Modes Tryptophan-Related Modes Histidine-Related Modes Cysteine-Related Modes X-Proline Vibrational Modes Modes of Metal-Coordinated Residues Visible Resonance Raman Spectra of Proteins Heme Proteins Heme Skeletal Vibrational Modes FeHis and FeCys stretching modes Fe(II)-O2 Related Modes Fe(II)-CO Related Modes Fe(III)-CN Related Modes Fe(II)-NO and Fe(III)-NO Related Modes Fe(III)-OH Related Modes Fe(IV)O Related Modes Copper Proteins Quinone Vibrations of Quinoproteins Tyrosine Radical Modes in Proteins Flavo Proteins VisRR Spectra of Other Proteins